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Titolo:
Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein
Autore:
Wigley, WC; Stidham, RD; Smith, NM; Hunt, JF; Thomas, PJ;
Indirizzi:
Univ Texas, SW Med Ctr, Dept Physiol, Dallas, TX 75235 USA Univ Texas Dallas TX USA 75235 ed Ctr, Dept Physiol, Dallas, TX 75235 USA Univ Texas, SW Med Ctr, Grad Program Mol Biophys, Dallas, TX 75235 USA Univ Texas Dallas TX USA 75235 Program Mol Biophys, Dallas, TX 75235 USA Columbia Univ, Dept Biol Sci, New York, NY 10027 USA Columbia Univ New York NY USA 10027 Dept Biol Sci, New York, NY 10027 USA
Titolo Testata:
NATURE BIOTECHNOLOGY
fascicolo: 2, volume: 19, anno: 2001,
pagine: 131 - 136
SICI:
1087-0156(200102)19:2<131:PSAFMI>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSMEMBRANE CONDUCTANCE REGULATOR; MALTOSE-BINDING PROTEIN; ESCHERICHIA-COLI; IN-VIVO; CYSTIC-FIBROSIS; BETA-GALACTOSIDASE; WILD-TYPE; DISEASE; FRAGMENTS; MUTATION;
Keywords:
aggregation; folding; solubility; complementation; protein-folding diseases;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
59
Recensione:
Indirizzi per estratti:
Indirizzo: Thomas, PJ Univ Texas, SW Med Ctr, Dept Physiol, 5323 Harry Hines Blvd, Dallas, TX 75235 USA Univ Texas 5323 Harry Hines Blvd Dallas TX USA 75235 75235 USA
Citazione:
W.C. Wigley et al., "Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein", NAT BIOTECH, 19(2), 2001, pp. 131-136

Abstract

Protein misfolding is the basis of a number of human diseases and presentsan obstacle to the production of soluble recombinant proteins. We present a general method to assess the solubility and folding of proteins in vivo. The basis of this assay is structural complementation between the alpha- and omega -fragments of beta -galactosidase (beta -gal). Fusions of the alpha-fragment to the C terminus of target proteins with widely varying in vivofolding yield and/or solubility levels, including the Alzheimer's amyloid beta (A beta) peptide and a non-amyloidogenic mutant thereof, reveal an unambiguous correlation between beta -gal activity and the solubility/folding of the target. Thus, structural complementation provides a means of monitoring protein solubility/misfolding in vivo, and should find utility in the screening for compounds that influence the pathological consequences of these processes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 11:51:40